Extensions to Michaelis-Menten Kinetics for Single Parameters
نویسندگان
چکیده
منابع مشابه
Single-molecule Michaelis-Menten equations.
This paper summarizes our present theoretical understanding of single-molecule kinetics associated with the Michaelis-Menten mechanism of enzymatic reactions. Single-molecule enzymatic turnover experiments typically measure the probability density f(t) of the stochastic waiting time t for individual turnovers. While f(t) can be reconciled with ensemble kinetics, it contains more information tha...
متن کاملOne hundred years of Michaelis–Menten kinetics
0.1016/j.pisc.2014 he Author. Publish mons.org/licenses t of an special issu etics”. Copyright thor. [email protected] Abstract The year 2013 marked the centenary of the paper of Leonor Michaelis and Maud Menten (Michaelis and Menten, 1913), and the 110th anniversary of the doctoral thesis of Victor Henri (Henri, 1903). These publications have had an enormous influence on the progress of biochem...
متن کاملReexamining Michaelis-Menten enzyme kinetics for xanthine oxidase.
Abbreviated expressions for enzyme kinetic expressions, such as the Michaelis-Menten (M-M) equations, are based on the premise that enzyme concentrations are low compared with those of the substrate and product. When one does progress experiments, where the solute is consumed during conversion to form a series of products, the idealized conditions are violated. Here, we analyzed data of xanthin...
متن کاملSingle-molecule enzymology à la Michaelis-Menten.
Over the past 100 years, deterministic rate equations have been successfully used to infer enzyme-catalysed reaction mechanisms and to estimate rate constants from reaction kinetics experiments conducted in vitro. In recent years, sophisticated experimental techniques have been developed that begin to allow the measurement of enzyme-catalysed and other biopolymer-mediated reactions inside singl...
متن کاملParallel versus Off-Pathway Michaelis-Menten Mechanism for Single-Enzyme Kinetics of a Fluctuating Enzyme.
Recent fluorescence spectroscopy measurements of the turnover time distribution of single-enzyme turnover kinetics of β-galactosidase provide evidence of Michaelis-Menten kinetics at low substrate concentration. However, at high substrate concentrations, the dimensionless variance of the turnover time distribution shows systematic deviations from the Michaelis-Menten prediction. This difference...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Scientific Reports
سال: 2018
ISSN: 2045-2322
DOI: 10.1038/s41598-018-34675-2